A broad glass transition in hydrated proteins |
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Authors: | S. Khodadadi A. MalkovskiyA. Kisliuk A.P. Sokolov |
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Affiliation: | Department of Polymer Science, University of Akron, Akron, OH 44325, USA |
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Abstract: | We performed Raman and Brillouin scattering measurements to estimate glass transition temperature, Tg, of hydrated protein. The measurements reveal very broad glass transition in hydrated lysozyme with approximate Tg ∼ 180 ± 15 K. This result agrees with a broad range of Tg ∼ 160–200 K reported in literature for hydrated globular proteins and stresses the difference between behavior of hydrated biomolecules and simple glass-forming systems. Moreover, the main structural relaxation of the hydrated protein system that freezes at Tg ∼ 180 K remains unknown. We emphasize the difference between the “dynamic transition”, known as a sharp rise in mean-squared atomic displacement <r2> at temperatures around TD ∼ 200–230 K, and the glass transition. They have different physical origin and should not be confused. |
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Keywords: | Hydrated protein Glass transition temperature Dynamic transition Light scattering Dielectric spectroscopy |
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